630 IRF6 is required for directed cell migration in murine primary keratinocytes

During development, directed cell migration is crucial for achieving proper shape and function of organs. One well-studied example is the embryonic development of the larval tracheal system of Drosophila, in which at least four signaling pathways coordinate cell migration to form an elaborate branched network essential for oxygen delivery throughout the larva. FGF signaling is required for guided migration of all tracheal branches, whereas the DPP, EGF receptor, and Wingless/WNT signaling pathways each mediate the formation of specific subsets of branches. Here, we characterize ribbon, which encodes a BTB/POZ-containing protein required for specific tracheal branch migration. In ribbon mutant tracheae, the dorsal trunk fails to form, and ventral branches are stunted; however, directed migrations of the dorsal and visceral branches are largely unaffected. The dorsal trunk also fails to form when FGF or Wingless/WNT signaling is lost, and we show that ribbon functions downstream of, or parallel to, these pathways to promote anterior-posterior migration. Directed cell migration of the salivary gland and dorsal epidermis are also affected in ribbon mutants, suggesting that conserved mechanisms may be employed to orient cell migrations in multiple tissues during development.

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The atypical Rho GTPase RhoD is a regulator of actin cytoskeleton dynamics and directed cell migration

Experimental Cell Research ◽

10.1016/j.yexcr.2017.02.013 ◽

2017 ◽

Vol 352 (2) ◽

pp. 255-264 ◽

Cited By ~ 15

Author(s):

Magdalena Blom ◽

Katarina Reis ◽

Johan Heldin ◽

Johan Kreuger ◽

Pontus Aspenström

Keyword(s):

Cell Migration ◽

Actin Cytoskeleton ◽

Rho Gtpase ◽

Directed Cell Migration ◽

Cytoskeleton Dynamics

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Design and fabrication of engineered platforms to control multiple cue directed cell migration

10.31274/etd-180810-3732 ◽

2014 ◽

Author(s):

Laura M. Lara-Rodriguez

Keyword(s):

Cell Migration ◽

Directed Cell Migration

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Paxillin-Kinase-Linker Tyrosine Phosphorylation Regulates Directional Cell Migration

Molecular Biology of the Cell ◽

10.1091/mbc.e09-07-0548 ◽

2009 ◽

Vol 20 (22) ◽

pp. 4706-4719 ◽

Cited By ~ 39

Author(s):

Jianxin A. Yu ◽

Nicholas O. Deakin ◽

Christopher E. Turner

Keyword(s):

Cell Migration ◽

Cell Adhesion ◽

Growth Factor ◽

Tyrosine Phosphorylation ◽

Wound Repair ◽

Cell Polarization ◽

Dependent Manner ◽

Directed Cell Migration ◽

Focal Adhesion Protein ◽

Directional Cell Migration

Directed cell migration requires the coordination of growth factor and cell adhesion signaling and is of fundamental importance during embryonic development, wound repair, and pathological conditions such as tumor metastasis. Herein, we demonstrate that the ArfGAP, paxillin-kinase-linker (PKL/GIT2), is tyrosine phosphorylated in response to platelet-derived growth factor (PDGF) stimulation, in an adhesion dependent manner and is necessary for directed cell migration. Using a combination of pharmacological inhibitors, knockout cells and kinase mutants, FAK, and Src family kinases were shown to mediate PDGF-dependent PKL tyrosine phosphorylation. In fibroblasts, expression of a PKL mutant lacking the principal tyrosine phosphorylation sites resulted in loss of wound-induced cell polarization as well as directional migration. PKL phosphorylation was necessary for PDGF-stimulated PKL binding to the focal adhesion protein paxillin and expression of paxillin or PKL mutants defective in their respective binding motifs recapitulated the polarization defects. RNA interference or expression of phosphorylation mutants of PKL resulted in disregulation of PDGF-stimulated Rac1 and PAK activities, reduction of Cdc42 and Erk signaling, as well as mislocalization of βPIX. Together these studies position PKL as an integral component of growth factor and cell adhesion cross-talk signaling, controlling the development of front–rear cell polarity and directional cell migration.

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Effect of shear stress upon localization of the Golgi apparatus and microtubule organizing center in isolated cultured endothelial cells

Journal of Cell Science ◽

10.1242/jcs.104.4.1145 ◽

1993 ◽

Vol 104 (4) ◽

pp. 1145-1153 ◽

Cited By ~ 3

Author(s):

D.E. Coan ◽

A.R. Wechezak ◽

R.F. Viggers ◽

L.R. Sauvage

Keyword(s):

Endothelial Cells ◽

Shear Stress ◽

Cell Migration ◽

Golgi Apparatus ◽

Flow Direction ◽

Microtubule Organizing Center ◽

Directed Cell Migration ◽

Time Period ◽

Significant Difference ◽

Organizing Center

Despite substantial evidence to suggest that directed cell migration is dependent upon positioning of the Golgi apparatus (GA) and the microtubule organizing center (MTOC), some controversy exists about whether such a relationship is relevant to endothelial cells under flow. The present study was undertaken to provide an indepth investigation of the relationship between shear stress, GA/MTOC localization, cell migration and nuclear position. Bovine carotid endothelial cells were exposed to 22 or 88 dynes/cm2 for 0.5, 2, 8 or 24 h, and localization of their GA/MTOCs was determined relative to the direction of flow. In no-flow control specimens, (0, 0.5, 2, 8 and 24 h) there was no change in the equally distributed GA/MTOCs. In contrast, during the first 8 h at 88 dynes/cm2 and by 2 h at 22 dynes/cm2 there was a significant increase in the number of cells with GA/MTOCs localized upstream to flow direction. The effect was temporary, however, and by 24 h there was no significant difference between the no-flow, 22 and 88 dynes/cm2 specimens. Analysis of GA/MTOC localization with respect to the direction of cell migration determined that 72.5% of no-flow cells possessed GA/MTOCs localized to the sides of nuclei nearest the direction of migration. In contrast, 64% of the specimens shear stressed over the same time period had GA/MTOCs localized to the sides of nuclei opposite the direction of migration. These results suggest that positioning of the GA/MTOC in endothelial cells is not dependent completely upon the direction of migration.(ABSTRACT TRUNCATED AT 250 WORDS)

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